Rational design of coagulation factor VIIa variants with substantially increased intrinsic activity.
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Mechanism of the Ca2+-induced Enhancement of the Intrinsic Factor VIIa ActivityRezymogenation of active urokinase induced by an inhibitory antibodyThe consensus-based approach for gene/enzyme replacement therapies and crystallization strategies: the case of human alanine-glyoxylate aminotransferaseDisulfide locked variants of factor VIIa with a restricted beta-strand conformation have enhanced enzymatic activityRecombinant factor VIIa analog in the management of hemophilia with inhibitors: results from a multicenter, randomized, controlled trial of vatreptacog alfa.The endothelial protein C receptor supports tissue factor ternary coagulation initiation complex signaling through protease-activated receptors.Recombinant factor VIIa analog NN1731 (V158D/E296V/M298Q-FVIIa) enhances fibrin formation, structure and stability in lipidated hemophilic plasma.Utilizing the activation mechanism of serine proteases to engineer hepatocyte growth factor into a Met antagonistTherapy for haemophilia: recent advances and goals for the future.Structure-Function Relationship of the Interaction between Tissue Factor and Factor VIIa.Intravascular inhibition of factor VIIa and the analogue NN1731 by antithrombin.Proteases as therapeutics.Catalytic domain modification and viral gene delivery of activated factor VII confers hemostasis at reduced expression levels and vector doses in vivo.Molecular Basis of Enhanced Activity in Factor VIIa-Trypsin Variants Conveys Insights into Tissue Factor-mediated Allosteric Regulation of Factor VIIa ActivityAn activated factor VII variant with enhanced tissue factor-independent activity speeds wound healing in a mouse hemophilia B model.Non-canonical proteolytic activation of human prothrombin by subtilisin from Bacillus subtilis may shift the procoagulant-anticoagulant equilibrium toward thrombosis.The P303T mutation in the human factor VII (FVII) gene alters the conformational state of the enzyme and causes a severe functional deficiency.Augmented intrinsic activity of Factor VIIa by replacement of residues 305, 314, 337 and 374: evidence of two unique mutational mechanisms of activity enhancement.Factor VII mutant V154G models a zymogen-like form of factor VIIa.A combined structural dynamics approach identifies a putative switch in factor VIIa employed by tissue factor to initiate blood coagulation.Phage-assisted continuous evolution of proteases with altered substrate specificity.Antibody-induced enhancement of factor VIIa activity through distinct allosteric pathways.The endothelial protein C receptor enhances hemostasis of FVIIa administration in hemophilic mice in vivo.The length of the linker between the epidermal growth factor-like domains in factor VIIa is critical for a productive interaction with tissue factor.Recombinant factor VIIa analog (vatreptacog alfa [activated]) for treatment of joint bleeds in hemophilia patients with inhibitors: a randomized controlled trial.Assignment of molecular properties of a superactive coagulation factor VIIa variant to individual amino acid changes.Phase I, randomized, double-blind, placebo-controlled, single-dose escalation study of the recombinant factor VIIa variant BAY 86-6150 in hemophilia.Effect of recombinant factor VIIa variant (NN1731) on platelet function, clot structure and force onset time in whole blood from healthy volunteers and haemophilia patients.TRUST trial: BAY 86-6150 use in haemophilia with inhibitors and assessment for immunogenicity.Post hoc assessment of the immunogenicity of bioengineered factor VIIa demonstrates the use of preclinical tools.Predicting dosing advantages of factor VIIa variants with altered tissue factor-dependent and lipid-dependent activities.Platelet binding and activity of a factor VIIa variant with enhanced tissue factor independent activity.Factor VIIa analogue (V158D/E296V/M298Q-FVIIa) normalises clot formation in whole blood from patients with severe haemophilia A.Enhanced in vitro procoagulant and antifibrinolytic potential of superactive variants of recombinant factor VIIa in severe hemophilia A.Tissue factor activates allosteric networks in factor VIIa through structural and dynamic changes.Engineering of a membrane-triggered activity switch in coagulation factor VIIa.Recombinant human factor VIIa (rFVIIa) in hemophilia: mode of action and evidence to date.Changes in the amino acid sequence of the recombinant human factor VIIa analog, vatreptacog alfa, are associated with clinical immunogenicity.Pharmacokinetics and pharmacodynamics of rFVIIa and new improved bypassing agents for the treatment of haemophilia.Tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity.
P2860
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P2860
Rational design of coagulation factor VIIa variants with substantially increased intrinsic activity.
description
2001 nî lūn-bûn
@nan
2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Rational design of coagulation ...... increased intrinsic activity.
@ast
Rational design of coagulation ...... increased intrinsic activity.
@en
type
label
Rational design of coagulation ...... increased intrinsic activity.
@ast
Rational design of coagulation ...... increased intrinsic activity.
@en
prefLabel
Rational design of coagulation ...... increased intrinsic activity.
@ast
Rational design of coagulation ...... increased intrinsic activity.
@en
P2860
P356
P1476
Rational design of coagulation ...... y increased intrinsic activity
@en
P2093
P2860
P304
13583-13588
P356
10.1073/PNAS.241339498
P407
P50
P577
2001-11-06T00:00:00Z